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Literature summary extracted from

  • Gromiha, M.M.
    Factors influencing the stability of alpha-helices and beta-strands in thermophilic ribonuclease H (2001), Prep. Biochem. Biotechnol., 31, 103-112.
    View publication on PubMed

General Stability

EC Number General Stability Organism
3.1.26.4 calculation of stability versus hydrophobicity and residue contacts Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.4 Thermus thermophilus
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thermophilic enzyme
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Subunits

EC Number Subunits Comment Organism
3.1.26.4 More determination of the stability of residues in different secondary structures, alpha-helices and beta-strands, of the enzyme, comparison of experimental and computational data, correlation of stability in alpha-helices and beta-strands Thermus thermophilus

Synonyms

EC Number Synonyms Comment Organism
3.1.26.4 ribonuclease H
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Thermus thermophilus
3.1.26.4 RNase H
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Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.26.4 additional information
-
structures and mechanism of thermostability Thermus thermophilus